Seminars in virologyPub Date : 2022-01-01Epub Date: 2022-01-04DOI: 10.1007/s41066-021-00304-z
Rishikesh Chaurasiya, Divya Jain
{"title":"Pythagorean fuzzy entropy measure-based complex proportional assessment technique for solving multi-criteria healthcare waste treatment problem.","authors":"Rishikesh Chaurasiya, Divya Jain","doi":"10.1007/s41066-021-00304-z","DOIUrl":"10.1007/s41066-021-00304-z","url":null,"abstract":"<p><p>With the increasing risk to human health and environmental issues, the selection of appropriate management and treatment of healthcare waste has become a major problem, especially in developing countries. There are various alternatives to dispose of health care waste. The important is to assess the best alternative among them. The assessment of each alternative should be done based on public health, psychological, economic, environmental, technological, and operational aspect. The selection of the best health care waste treatment (HCWT) alternative is a complicated, multi-criteria decision-making (MCDM) problem involving numerous disparate qualitative and quantitative features. Hence, in this research article, the MCDM method is presented for estimating and choosing the best alternative of HCWT by COPRAS technique in a Pythagorean fuzzy set (PFS). Here, in this paper, first of all, a new entropy measure on PFSs is proposed and its validity is studied. Thereafter, the MCDM technique Complex Proportional Assessment (COPRAS) is discussed in which the criteria weights are assessed by the proposed entropy measure and score function to enhance an efficacy and efficiency of the proposed technique. Furthermore, the above-defined technique is employed to resolve the real-life problem to obtain the best treatment alternative to disposal of the health care waste. Finally, sensitivity analysis is presented to rationale the proposed viewpoint for prioritizing HCWT alternatives.</p>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"7 1","pages":"917-930"},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8723817/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72749570","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cell Type-specific Gene Expression Profiling in the Mouse Liver.","authors":"Amber W Wang, Adam M Zahm, Kirk J Wangensteen","doi":"10.3791/60242","DOIUrl":"10.3791/60242","url":null,"abstract":"<p><p>Liver repopulation after injury is a crucial feature of mammals which prevents immediate organ failure and death after exposure of environmental toxins. A deeper understanding of the changes in gene expression that occur during repopulation could help identify therapeutic targets to promote the restoration of liver function in the setting of injuries. Nonetheless, methods to isolate specifically the repopulating hepatocytes are inhibited by a lack of cell markers, limited cell numbers, and the fragility of these cells. The development of translating ribosome affinity purification (TRAP) technology in conjunction with the Fah<sup>-/-</sup> mouse model to recapitulate repopulation in the setting of liver injury allows gene expression profiling of the repopulating hepatocytes. With TRAP, cell type-specific translating mRNA is rapidly and efficiently isolated. We developed a method that utilizes TRAP with affinity-based isolation of translating mRNA from hepatocytes that selectively express the green fluorescent protein (GFP)-tagged ribosomal protein (RP), GFP:RPL10A. TRAP circumvents the long time period required for fluorescence-activated cell sorting that could change the gene expression profile. Furthermore, since only the repopulating hepatocytes express the GFP:RPL10A fusion protein, the isolated mRNA is devoid of contamination from the surrounding injured hepatocytes and other cell types in the liver. The affinity-purified mRNA is of high quality and allows downstream PCR- or high-throughput sequencing-based analysis of gene expression.</p>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 1","pages":""},"PeriodicalIF":1.2,"publicationDate":"2019-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7507956/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72755825","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Mathieu H.M. Noteborn, Astrid A.A.M. Danen-van Oorschot, Alex J. van der Eb
{"title":"Chicken Anemia Virus: Induction of Apoptosis by a Single Protein of a Single-Stranded DNA Virus","authors":"Mathieu H.M. Noteborn, Astrid A.A.M. Danen-van Oorschot, Alex J. van der Eb","doi":"10.1006/smvy.1998.0154","DOIUrl":"10.1006/smvy.1998.0154","url":null,"abstract":"<div><p>Chicken anemia virus (CAV) is a globally distributed avian pathogen. CAV has a circular single-stranded DNA of 2.3 kb and constitutes a unique type in the newly described virus family of<em>Circoviridae.</em>The CAV genome contains three partially or completely overlapping genes. CAV causes fatal cytopathogenic effects in chicken thymocytes and cultured transformed mononuclear cells via apoptosis. In transformed (chicken) cells, the synthesis of the VP3 gene product apoptin alone mimics this CAV-induced apoptosis, which is p53 independent and cannot be inhibited by the apoptosis-inhibiting proteins Bcl-2 and CrmA. Apoptin induces apoptosis in human tumor cells but, interestingly, not in normal cells. These properties suggest that apoptin may have potential medical applications.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 6","pages":"Pages 497-504"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1998.0154","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51142414","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Adenovirus E3 Proteins: 14.7K, RID, and gp19K Inhibit Immune-Induced Cell Death; Adenovirus Death Protein Promotes Cell Death","authors":"William S.M. Wold , Ann E. Tollefson","doi":"10.1006/smvy.1998.0156","DOIUrl":"10.1006/smvy.1998.0156","url":null,"abstract":"<div><p>The adenovirus E3 transcription unit encodes proteins named E3-14.7K, RID, and E3-gp19K that prevent killing of infected cells by the host immune system. Tumor necrosis factor (TNF), a cytokine secreted by activated monocytes and cytotoxic T lymphocytes (CTL), can induce apoptosis when it engages the TNF receptor on target cells. E3-14.7K and RID independently prevent TNF-induced apoptosis. Fas ligand, which is expressed on activated CTL and natural killer cells, induces apoptosis when it engages its receptor, Fas, on target cells. RID blocks apoptosis through Fas by stimulating the clearance of Fas from the infected cell surface and its degradation in lysosomes. CTL induce apoptosis when the T cell receptor engages the MHC class I antigen–peptide complex on target cells. E3-gp19K inhibits killing by CTL by blocking transport of MHC class I antigens to the infected cell surface. After virus replication is complete, the cell lyses and releases virus particles; this cell lysis is mediated by the E3-coded adenovirus death protein.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 6","pages":"Pages 515-523"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1998.0156","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51142525","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"INTRODUCTION: Apoptosis in Virus Infection","authors":"Lois K. Miller, Eileen White","doi":"10.1006/smvy.1998.0148","DOIUrl":"10.1006/smvy.1998.0148","url":null,"abstract":"","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 6","pages":"Pages 443-444"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1998.0148","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51142691","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Modulation of Apoptosis by Herpesviruses","authors":"Elliott Kieff , Thomas Shenk","doi":"10.1006/smvy.1998.0151","DOIUrl":"10.1006/smvy.1998.0151","url":null,"abstract":"<div><p>The herpesvirus family of viruses is large, containing over 100 different members, of which 8 infect humans. In this short review, we examine the induction and inhibition of apoptosis by herpesviruses, focusing primarily on the human viruses.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 6","pages":"Pages 471-480"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1998.0151","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51142326","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Regulation of Apoptosis by Adenovirus E1A and E1B Oncogenes","authors":"Eileen White","doi":"10.1006/smvy.1998.0155","DOIUrl":"10.1006/smvy.1998.0155","url":null,"abstract":"<div><p>Adenovirus E1A promotes apoptosis by interacting with and inhibiting negative regulators of cell cycle control. Binding of E1A to, and inhibition of, the transcriptional coadaptor p300 promotes accumulation of the p53 tumor suppressor protein which induces apoptosis. By inhibiting p300, E1A prevents the transcriptional activation of<em>mdm-2,</em>the product of which interacts with and promotes the degradation of p53. Thus the E1A–p300 interaction disables the negative feedback loop to control p53 levels, which left unrestrained, cause apoptosis rather than growth arrest. The E1B 19K protein functions analogously to Bcl-2 to inhibit apoptosis by E1A, p53, and multiple other stimuli. The E1B 19K protein functions by at least two independent mechanisms to inhibit apoptosis. First, the E1B 19K protein binds to the pro-apoptotic Bax protein to prevent loss of mitochondrial membrane potential, caspase activation, and apoptosis. Second, the E1B 19K protein inhibits caspase interaction by interfering with the function of adaptor molecules such as FADD and Ced-4 that interact with and activate caspases. By inhibiting FADD-dependent activation of the caspase FLICE, the E1B 19K protein can disable both the TNF-α- and the Fas-mediated death signaling pathways which play an important role in immune surveillance against virus infection and cancer. The E1B 19K protein binds to Ced-4, and presumably mammalian Ced-4 homologues, and thereby prevents caspase activation. Thus, the study of the mechanism of regulation of apoptosis by the adenovirus transforming proteins has revealed important regulatory steps in death signaling pathways.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 6","pages":"Pages 505-513"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1998.0155","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51142463","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Lois K. Miller, William J. Kaiser, Somasekar Seshagiri
{"title":"Baculovirus Regulation of Apoptosis","authors":"Lois K. Miller, William J. Kaiser, Somasekar Seshagiri","doi":"10.1006/smvy.1998.0149","DOIUrl":"10.1006/smvy.1998.0149","url":null,"abstract":"<div><p>The baculovirus AcMNPV induces apoptosis in a host-specific manner which involves the activation of host caspases (cysteine-dependent, aspartate-specific proteases). AcMNPV carries a novel gene, p35, which encodes a stoichiometric inhibitor of active caspases, thereby blocking apoptosis. P35 is cleaved by caspases and the cleavage products form a stable complex with the caspase. Baculoviruses also carry genes known as iaps (inhibitors of apoptosis), some of which can actively suppress apoptosis by inhibiting the activation of caspases. Members of the IAP family are found in both viral and animal genomes and interact physically with a variety of proteins associated with apoptotic pathways including Reaper, Doom, TRAF2, and some caspases. The ability of baculoviruses to block apoptosis influences their pathogenicity and host range.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 6","pages":"Pages 445-452"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1998.0149","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51142765","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Author Index for Volume 8","authors":"","doi":"10.1006/smvy.1998.0157","DOIUrl":"https://doi.org/10.1006/smvy.1998.0157","url":null,"abstract":"","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 6","pages":"Pages 524-525"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1998.0157","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"134670734","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Stacey Schultz-Cherry , Robert M. Krug , Virginia S. Hinshaw
{"title":"Induction of Apoptosis by Influenza Virus","authors":"Stacey Schultz-Cherry , Robert M. Krug , Virginia S. Hinshaw","doi":"10.1006/smvy.1998.0153","DOIUrl":"10.1006/smvy.1998.0153","url":null,"abstract":"<div><p>It has been postulated that virus-induced apoptosis is an important factor in pathogenesis caused by cytopathogenic viruses. Apoptosis is induced by both influenza A and influenza B viruses, which are cytopathogenic negative-strand RNA viruses. The importance of influenza viruses as worldwide pathogens in humans and domestic animals is well recognized. In this report, we review the current state of knowledge of the mechanism(s) of influenza virus-induced apoptosis. Several cellular factors and at least one virus-specific protein, the nonstructural protein NS1, have been implicated in influenza virus-induced apoptosis. However, the mechanism(s) of influenza virus-induced apoptosis are not well understood at the present time.</p></div>","PeriodicalId":92955,"journal":{"name":"Seminars in virology","volume":"8 6","pages":"Pages 491-495"},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/smvy.1998.0153","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51142373","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}